T23O_HUMAN - dbPTM
T23O_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID T23O_HUMAN
UniProt AC P48775
Protein Name Tryptophan 2,3-dioxygenase {ECO:0000255|HAMAP-Rule:MF_03020}
Gene Name TDO2 {ECO:0000255|HAMAP-Rule:MF_03020}
Organism Homo sapiens (Human).
Sequence Length 406
Subcellular Localization
Protein Description Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety..
Protein Sequence MSGCPFLGNNFGYTFKKLPVEGSEEDKSQTGVNRASKGGLIYGNYLHLEKVLNAQELQSETKGNKIHDEHLFIITHQAYELWFKQILWELDSVREIFQNGHVRDERNMLKVVSRMHRVSVILKLLVQQFSILETMTALDFNDFREYLSPASGFQSLQFRLLENKIGVLQNMRVPYNRRHYRDNFKGEENELLLKSEQEKTLLELVEAWLERTPGLEPHGFNFWGKLEKNITRGLEEEFIRIQAKEESEEKEEQVAEFQKQKEVLLSLFDEKRHEHLLSKGERRLSYRALQGALMIYFYREEPRFQVPFQLLTSLMDIDSLMTKWRYNHVCMVHRMLGSKAGTGGSSGYHYLRSTVSDRYKVFVDLFNLSTYLIPRHWIPKMNPTIHKFLYTAEYCDSSYFSSDESD
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
23PhosphorylationKKLPVEGSEEDKSQT
EECCCCCCCCHHHCC
25.0624275569
146PhosphorylationDFNDFREYLSPASGF
CHHHHHHHCCCCCCC
14.2816094384
155PhosphorylationSPASGFQSLQFRLLE
CCCCCCCHHHHHHHC
23.1316094384
200PhosphorylationLKSEQEKTLLELVEA
CHHHHHHHHHHHHHH
35.5024719451
212PhosphorylationVEAWLERTPGLEPHG
HHHHHHHCCCCCCCC
16.6024719451
231PhosphorylationGKLEKNITRGLEEEF
HHHHHHHCCCCHHHH
28.2521955146
369PhosphorylationFVDLFNLSTYLIPRH
HHHHHCCHHHHCCHH
18.99-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of T23O_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of T23O_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of T23O_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ASML_HUMANASMTLphysical
16189514
KDM1A_HUMANKDM1Aphysical
23455924
ANM6_HUMANPRMT6physical
23455924
ASML_HUMANASMTLphysical
24722188
T23O_HUMANTDO2physical
24722188
MEOX2_HUMANMEOX2physical
24722188
NMNA1_HUMANNMNAT1physical
24722188
REL_HUMANRELphysical
24722188
SDCB1_HUMANSDCBPphysical
24722188
T23O_HUMANTDO2physical
25416956
ASML_HUMANASMTLphysical
25416956
DPM1_HUMANDPM1physical
25416956
ZFY26_HUMANZFYVE26physical
25416956
SDCB2_HUMANSDCBP2physical
25416956
MOB1A_HUMANMOB1Aphysical
25416956
NGB_HUMANNGBphysical
25416956
MOB3C_HUMANMOB3Cphysical
25416956
ASML_HUMANASMTLphysical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00150L-Tryptophan
DB00779Nalidixic Acid
DB00500Tolmetin
Regulatory Network of T23O_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry.";
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
Nat. Methods 2:591-598(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND MASSSPECTROMETRY.

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